ID W7HK51_9PEZI Unreviewed; 314 AA.
AC W7HK51;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 22-FEB-2023, entry version 36.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=DRE_01207 {ECO:0000313|EMBL:EWC44381.1};
OS Drechslerella stenobrocha 248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Drechslerella.
OX NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC44381.1, ECO:0000313|Proteomes:UP000024837};
RN [1] {ECO:0000313|EMBL:EWC44381.1, ECO:0000313|Proteomes:UP000024837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=248 {ECO:0000313|EMBL:EWC44381.1,
RC ECO:0000313|Proteomes:UP000024837};
RA Liu X., Zhang W., Liu K.;
RT "Drechslerella stenobrocha genome reveals carnivorous origination and
RT mechanical trapping mechanism of predatory fungi.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; KI966443; EWC44381.1; -; Genomic_DNA.
DR AlphaFoldDB; W7HK51; -.
DR HOGENOM; CLU_013253_0_3_1; -.
DR Proteomes; UP000024837; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06097; Aspergillopepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF1; ASPARTYL PROTEINASE; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000024837}.
FT DOMAIN 2..311
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 18
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 197
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 314 AA; 33822 MW; CBE2BC167728C2D0 CRC64;
MYLSPVSIGG QKFNFDLDTG SSDLWVFSNK LPASIQRKHK SNGGKIYTPG PTAKNANGLT
WSITYVDNSG ASGTVVTDNV KIGGITVKKQ AVEVASRISA MFEDFEGDGL LVSPTKQQTW
FENAMSQLQS KLFTADLNQQ SAGSYGWGYI NSIYSKKIAY AKIRNTGWWH VDAGGGIRVN
GKLTTTGASY TAGAVPDTGT TLLLLPNSLV KLYYASVPKA QYSSEAGAWV YPCTPQGFPN
LPPLSIPVGK SWATIPGKYL TYAYANSAGT SCFGGLQGLS DSSDLPFIYG DIFFKANFAV
FDYGNKRFGF AQKR
//